ID   RNP1_METS3              Reviewed;          92 AA.
AC   A5UL80;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Ribonuclease P protein component 1 {ECO:0000255|HAMAP-Rule:MF_00754};
DE            Short=RNase P component 1 {ECO:0000255|HAMAP-Rule:MF_00754};
DE            EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00754};
DE   AltName: Full=Rpp29 {ECO:0000255|HAMAP-Rule:MF_00754};
GN   Name=rnp1 {ECO:0000255|HAMAP-Rule:MF_00754};
GN   OrderedLocusNames=Msm_0753;
OS   Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=420247;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX   PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA   Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA   Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT   "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT   human gut.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
CC   -!- FUNCTION: Part of ribonuclease P, a protein complex that generates
CC       mature tRNA molecules by cleaving their 5'-ends. {ECO:0000255|HAMAP-
CC       Rule:MF_00754}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC         from tRNA precursor.; EC=3.1.26.5; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00754};
CC   -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 protein
CC       subunits. {ECO:0000255|HAMAP-Rule:MF_00754}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00754}.
CC   -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein
CC       component 1 family. {ECO:0000255|HAMAP-Rule:MF_00754}.
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DR   EMBL; CP000678; ABQ86958.1; -; Genomic_DNA.
DR   RefSeq; WP_004033218.1; NZ_CP117965.1.
DR   AlphaFoldDB; A5UL80; -.
DR   SMR; A5UL80; -.
DR   STRING; 420247.Msm_0753; -.
DR   EnsemblBacteria; ABQ86958; ABQ86958; Msm_0753.
DR   GeneID; 78817382; -.
DR   KEGG; msi:Msm_0753; -.
DR   PATRIC; fig|420247.28.peg.750; -.
DR   eggNOG; arCOG00784; Archaea.
DR   HOGENOM; CLU_107020_2_1_2; -.
DR   Proteomes; UP000001992; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000172; C:ribonuclease MRP complex; IEA:InterPro.
DR   GO; GO:0030677; C:ribonuclease P complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0033204; F:ribonuclease P RNA binding; IEA:InterPro.
DR   GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.30.30.210; Ribonuclease P/MRP, subunit p29; 1.
DR   HAMAP; MF_00754; RNase_P_1; 1.
DR   InterPro; IPR016848; RNase_P/MRP_Rpp29-subunit.
DR   InterPro; IPR036980; RNase_P/MRP_Rpp29_sf.
DR   InterPro; IPR023538; RNP1.
DR   InterPro; IPR023534; Rof/RNase_P-like.
DR   InterPro; IPR002730; Rpp29/RNP1.
DR   PANTHER; PTHR13348:SF0; RIBONUCLEASE P PROTEIN SUBUNIT P29; 1.
DR   PANTHER; PTHR13348; RIBONUCLEASE P SUBUNIT P29; 1.
DR   Pfam; PF01868; RNase_P-MRP_p29; 1.
DR   SMART; SM00538; POP4; 1.
DR   SUPFAM; SSF101744; Rof/RNase P subunit-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Endonuclease; Hydrolase; Nuclease; tRNA processing.
FT   CHAIN           1..92
FT                   /note="Ribonuclease P protein component 1"
FT                   /id="PRO_1000046615"
SQ   SEQUENCE   92 AA;  10402 MW;  EEB468151514A9DC CRC64;
     MITVNNLVHH EFIGLSVSVT SVSNESLRLK GTVIDETKNT IKIEVDDNVE KIIPKKGSIF
     VFELPTGEKV EINGNILSIR PEDRIKKRFK KI
//